ID G8BPC1_TETPH Unreviewed; 2074 AA.
AC G8BPC1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=UvrD-like helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TPHA0B01790 {ECO:0000313|EMBL:CCE61852.1};
GN OrderedLocusNames=TPHA_0B01790 {ECO:0000313|EMBL:CCE61852.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE61852.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE61852.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE612857; CCE61852.1; -; Genomic_DNA.
DR RefSeq; XP_003684286.1; XM_003684238.1.
DR STRING; 1071381.G8BPC1; -.
DR GeneID; 11535006; -.
DR KEGG; tpf:TPHA_0B01790; -.
DR eggNOG; KOG1801; Eukaryota.
DR HOGENOM; CLU_000459_2_0_1; -.
DR OMA; PWHQSEL; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000005666; Chromosome 2.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR CDD; cd21408; 1B_Sen1p-like; 1.
DR CDD; cd18042; DEXXQc_SETX; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR044340; Helicase_Sen1_1B_dom.
DR InterPro; IPR024481; Helicase_Sen1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF12726; SEN1_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT DOMAIN 91..874
FT /note="Helicase Sen1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12726"
FT DOMAIN 1340..1632
FT /note="DNA2/NAM7 helicase helicase"
FT /evidence="ECO:0000259|Pfam:PF13086"
FT DOMAIN 1640..1839
FT /note="DNA2/NAM7 helicase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13087"
FT REGION 947..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..1977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2021..2074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1518..1545
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 954..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2058..2074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2074 AA; 237037 MW; F5061941FED29516 CRC64;
MNSSNRIISS TDNLYKYKEI AKQLAPKIEL VYSGKAPNSE ETIILKEVIS FLVSLPEGTH
LFCDEAFREI TIFSIVIFSF KQQTTIDYVT HYLVKSINTC EKCILQFIRG KNKILKHFAI
QRLVAYQHVT EFSDMVDKWR IPIVLKRLQD ITTVPSLAAA LSNSSGNNDE VDKKHLEIPR
DIQLAFFECL CNPKMLRLDK SLKGTFNAIF TFFLSLSLPL LNSYNSLINS ENLITNENNN
SETIVIPEFI AGIIYCWYEG KPDQSNWAKG VLVYLQSKQF KFKVDTITFD IIEEINFHNV
YLQDPSNWNH INISRFWLKF SAILTFMELP VIKEYFELPK NIQSLRQTYK NFTIESIFKL
WYNHLASPYQ MKPTSILLRA FNMFLEIYKH DFWGKVDPYT FHSVLDTIFA KDSYVIDLIQ
VENNADDDDD TIFLDYGTLS DMVTWTISFY HSVSDSKKIQ MIKKVSTIFL NFIAKKTSSN
GLTNACFFNS SAALLSYVLV IKENERGLLY EKDDFETILF TKIDFRIFLN NPLIQDVFIR
TITNPADLYL NLDSYLSTLS SSAMEVISKC ISLEILLLCH YSFKLYSGKN ITDSSSSFIL
LKNLTDNLSL TSFQDGPALA KQVLISFRDI NGLLEVSVKT QMVQNHNTKV SNFLKLSTKL
LEKCTDVSPQ HMSEILKDNG VAQGFWSCVF SPNDDLYQAA TNILYDTFDV EGRLEGIQEI
LQTNLTGHIR AINLVLTHLI KCEFFESCPR AVRVLMDIVN TCTDPTSGII SNFLTLKDDM
TIIEFRKLWN LVWIFLDTIY KCTLRWASKY EYSELENFTK DTLELSRSLI DSYGEFSTVL
NQDDDVMFNS VLSAIKNMLY WLRLSDDQLL ESCVHLISST SDLANKKGIK FNDTLVEMMT
RYALKAKKYS NKLTEQQSNE ILTKAKLFND KLTASVKESV ESYRKEKDLS RQTLLQKSKQ
PIELTPTSSS PESRADFLQR KAMASSITGR PKGSQSKLTS FGSFQSTHSP TLQGIKTTSA
PPLSKMEIAR RQLLNNRVVH PPSDSVFRSK HISVKRNDSS SDESELDIES ARELFATAKS
KKGIQTLDIN GKQIKRQTEA ERVKMEEEYM RKRLNIDINP FYNSILKWDY NRKDEFPDEK
QLNEYSPVKD VYNSVEEYQS IMRSLLLLET WQGLCSARDR EEYTPFPIIV GNRVAVSDFY
EIYASVKKSK LTEANISESD MVVLAYLSDV QYGEKLKKAH FQRAQHTCLA KIKTLKNAKN
DNVDVTLRIH RSQTFTKYLT LRSEIQAMKV MQMTTVEREY TSLEGLQYYD LVPQILAANP
ASPPDVSTGE IEEVKRNYSL NDSQAMAVVN TVAADGFSLI QGPPGTGKTK TILGIVGHIL
TTQDALPKNI IKVPGEQNSS PALEQTLKRK KVLICAPSNA AVDEICLRLR NGIATNNGNP
FLLSVVRIGR SDAVNAAIKD LTLEELVEKK VSEKNYNMTS NPDLERKFSS CVTKRRAARA
KLDSENGAID STMSTEEITN LQLEIRELSK QINQLGKERD EIREQNSINY RNRELDRRNA
QARVLANSNI ICSTLSGSAH DVLSTLGVKF DTVIIDEACQ CTELSAIIPL RYGAKRCIMV
GDPNQLPPTV LSSKASSLNY DQSLFVRMEK KCSPYLLNVQ YRMHPSISAF PSLEFYDGKL
KDGPDMANIT KRPWHSIDSL GPYKFFDIIS GRHEQNSRTM SYNNPEEARV AVELVDFLLK
RFENKYDFTG KIGVISPYKE QVFKLRREFR NHFGLLIEKY VDFNTIDGFQ GQEKEIIILS
CVRANDSDHA SGVGFLKDFR RMNVAFTRAK SSLWILGHHR SLKRDKLWNH LITNAKQRNK
LELACSGFLD INNTRVIKIL EHYKDSHNYI GGDDDYSPVS RYDNESNNSK RKLKEIKNST
PMNENVKKQK HSREIVAPNP LRPAAKKKSS IFNKSKLDEV KSQRSSKKKS SIFGGPTIGE
TISKTVVPYI KDKTIKNDVN KKNKKDNRTV RISDDITIIE DKHHYDDDDD EAEDEYDPLA
SEKYNLPTVN HIKRLHSPPL PKPSEDEDPY VPHT
//
